AATP4_ARATH
ID AATP4_ARATH Reviewed; 491 AA.
AC F4IJ77; Q9ZPX7;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=AAA-ATPase At2g46620;
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
GN OrderedLocusNames=At2g46620 {ECO:0000312|EMBL:AEC10730.1};
GN ORFNames=F13A10.15 {ECO:0000312|EMBL:AAD20172.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-491.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL77654.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006418; AAD20172.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10730.1; -; Genomic_DNA.
DR EMBL; AY075646; AAL77654.1; ALT_INIT; mRNA.
DR EMBL; AY143966; AAN28905.1; -; mRNA.
DR PIR; B84905; B84905.
DR RefSeq; NP_182185.2; NM_130227.4.
DR AlphaFoldDB; F4IJ77; -.
DR SMR; F4IJ77; -.
DR STRING; 3702.AT2G46620.1; -.
DR iPTMnet; F4IJ77; -.
DR PaxDb; F4IJ77; -.
DR PRIDE; F4IJ77; -.
DR ProteomicsDB; 244621; -.
DR EnsemblPlants; AT2G46620.1; AT2G46620.1; AT2G46620.
DR GeneID; 819274; -.
DR Gramene; AT2G46620.1; AT2G46620.1; AT2G46620.
DR KEGG; ath:AT2G46620; -.
DR Araport; AT2G46620; -.
DR TAIR; locus:2039981; AT2G46620.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_0_4_1; -.
DR InParanoid; F4IJ77; -.
DR OMA; HVYQFLT; -.
DR OrthoDB; 532729at2759; -.
DR PRO; PR:F4IJ77; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IJ77; baseline and differential.
DR Genevisible; F4IJ77; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025753; AAA_N_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14363; AAA_assoc; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="AAA-ATPase At2g46620"
FT /id="PRO_0000434706"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 423..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 491 AA; 55910 MW; 53CC00C0F336FA2F CRC64;
MGILWDSFLL LLVSTFALFL VRILLFKTGL IYMVKLWRRK IIDWFHVYQF YKVPEFNDNV
QENHLYQKVY MYLNSLSSIE NSDFTNLFTG KKSNEIILRL DRNQVVGDEF LGARVCWING
EDEDGARNFV LKIRKADKRR ILGSYLQHIH TVSDELEQRN TELKLFINVG IDDHLNKKKK
KNGRWRSIPF DHPCTFDNIA METDLKNKVK SDLESFLKGK QYYNRLGRVW KRSYLLYGPS
GTGKSSFVAA MANFLDYDVY DIDLSKVVDD SDLKMLLLQT RGKSVIVIED LDRHLSTKST
AVNLSGILNF TDSILSSCTA DERIMVFTMT GKEQIDPAML RPGRVDVHIH FPLCDFTAFK
TLANNYLGVK EHKLFSQVEG IFQNGASLSP AEIGELMIAN RNSPTRALKH VINALQTDGD
RRGTGRRLLL ENGSRKSTSE DVSDDMSGSL CGGGGGSSPA VKEFRKLYGL LRIKSSRKSG
SFDVAREMRD G
